RAB6B_MOUSE
ID RAB6B_MOUSE Reviewed; 208 AA.
AC P61294;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ras-related protein Rab-6B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:Q9NRW1};
GN Name=Rab6b; Synonyms=D9Bwg0185e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP INTERACTION WITH BICDL1.
RX PubMed=20360680; DOI=10.1038/emboj.2010.51;
RA Schlager M.A., Kapitein L.C., Grigoriev I., Burzynski G.M., Wulf P.S.,
RA Keijzer N., de Graaff E., Fukuda M., Shepherd I.T., Akhmanova A.,
RA Hoogenraad C.C.;
RT "Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related
RT protein 1 (BICDR-1) regulates neuritogenesis.";
RL EMBO J. 29:1637-1651(2010).
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between active GTP-bound and inactive
CC GDP-bound states. In their active state, drive transport of vesicular
CC carriers from donor organelles to acceptor organelles to regulate the
CC membrane traffic that maintains organelle identity and morphology.
CC Regulates the compacted morphology of the Golgi. Seems to have a role
CC in retrograde membrane traffic at the level of the Golgi complex. May
CC function in retrograde transport in neuronal cells.
CC {ECO:0000250|UniProtKB:Q9NRW1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:Q9NRW1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:Q9NRW1};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. {ECO:0000250|UniProtKB:Q9NRW1}.
CC -!- SUBUNIT: Interacts with RAB6KIFL. Interacts (GTP-bound) with BICD1 (via
CC C-terminus); the interaction is direct. Interacts (GDP-bound) with
CC DYNLRB1 (By similarity). Interacts with BICDL1/BICDR1; leads to its
CC accumulation in the pericentrosomal region. Interacts (GTP-bound) with
CC APBA1/MINT1 isoform 3, also called Mint1_826 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P61294; A0JNT9: Bicdl1; NbExp=2; IntAct=EBI-529766, EBI-7893170;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9NRW1}; Lipid-anchor {ECO:0000305}. Endoplasmic
CC reticulum-Golgi intermediate compartment
CC {ECO:0000250|UniProtKB:Q9NRW1}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q9NRW1}. Note=Colocalizes with BICD1 at
CC vesicular structures that align along microtubules.
CC {ECO:0000250|UniProtKB:Q9NRW1}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AK035893; BAC29230.1; -; mRNA.
DR EMBL; BC060618; AAH60618.1; -; mRNA.
DR CCDS; CCDS23449.1; -.
DR RefSeq; NP_776142.1; NM_173781.4.
DR AlphaFoldDB; P61294; -.
DR SMR; P61294; -.
DR BioGRID; 234782; 13.
DR IntAct; P61294; 13.
DR MINT; P61294; -.
DR STRING; 10090.ENSMUSP00000035155; -.
DR iPTMnet; P61294; -.
DR PhosphoSitePlus; P61294; -.
DR SwissPalm; P61294; -.
DR jPOST; P61294; -.
DR PaxDb; P61294; -.
DR PeptideAtlas; P61294; -.
DR PRIDE; P61294; -.
DR ProteomicsDB; 300383; -.
DR ABCD; P61294; 21 sequenced antibodies.
DR Antibodypedia; 46687; 187 antibodies from 24 providers.
DR DNASU; 270192; -.
DR Ensembl; ENSMUST00000035155; ENSMUSP00000035155; ENSMUSG00000032549.
DR GeneID; 270192; -.
DR KEGG; mmu:270192; -.
DR UCSC; uc009rgf.1; mouse.
DR CTD; 51560; -.
DR MGI; MGI:107283; Rab6b.
DR VEuPathDB; HostDB:ENSMUSG00000032549; -.
DR eggNOG; KOG0094; Eukaryota.
DR GeneTree; ENSGT00940000159656; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P61294; -.
DR OMA; TRFVYDH; -.
DR OrthoDB; 1277051at2759; -.
DR PhylomeDB; P61294; -.
DR TreeFam; TF300803; -.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 270192; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Rab6b; mouse.
DR PRO; PR:P61294; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P61294; protein.
DR Bgee; ENSMUSG00000032549; Expressed in substantia nigra and 221 other tissues.
DR ExpressionAtlas; P61294; baseline and differential.
DR Genevisible; P61294; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1903292; P:protein localization to Golgi membrane; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..208
FT /note="Ras-related protein Rab-6B"
FT /id="PRO_0000121116"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 208
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 206
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 208
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 208 AA; 23462 MW; E81C831996E2446D CRC64;
MSAGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR
TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNLNS FQQTSKWIDD VRTERGSDVI
IMLVGNKTDL ADKRQITIEE GEQRAKELSV MFIETSAKTG YNVKQLFRRV ASALPGMENV
QEKSKEGMID IKLDKPQEPP ASEGGCSC
